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YcgC represents a new protein deacetylase family in prokaryotes

Authors :
Shun Tu
Shu-Juan Guo
Chien-Sheng Chen
Cheng-Xi Liu
He-Wei Jiang
Feng Ge
Jiao-Yu Deng
Yi-Ming Zhou
Daniel M Czajkowsky
Yang Li
Bang-Ruo Qi
Young-Hoon Ahn
Philip A Cole
Heng Zhu
Sheng-Ce Tao
Source :
eLife, Vol 4 (2015)
Publication Year :
2015
Publisher :
eLife Sciences Publications Ltd, 2015.

Abstract

Reversible lysine acetylation is one of the most important protein posttranslational modifications that plays essential roles in both prokaryotes and eukaryotes. However, only a few lysine deacetylases (KDACs) have been identified in prokaryotes, perhaps in part due to their limited sequence homology. Herein, we developed a ‘clip-chip’ strategy to enable unbiased, activity-based discovery of novel KDACs in the Escherichia coli proteome. In-depth biochemical characterization confirmed that YcgC is a serine hydrolase involving Ser200 as the catalytic nucleophile for lysine deacetylation and does not use NAD+ or Zn2+ like other established KDACs. Further, in vivo characterization demonstrated that YcgC regulates transcription by catalyzing deacetylation of Lys52 and Lys62 of a transcriptional repressor RutR. Importantly, YcgC targets a distinct set of substrates from the only known E. coli KDAC CobB. Analysis of YcgC’s bacterial homologs confirmed that they also exhibit KDAC activity. YcgC thus represents a novel family of prokaryotic KDACs.

Details

Language :
English
ISSN :
2050084X
Volume :
4
Database :
Directory of Open Access Journals
Journal :
eLife
Publication Type :
Academic Journal
Accession number :
edsdoj.5925812ffa624314bc7972dcd4a3cd93
Document Type :
article
Full Text :
https://doi.org/10.7554/eLife.05322